title: Identification of the major protein adduct formed in rat liver after thioacetamide administration.
abstract: The in vivo covalent binding of the hepatocarcinogen thioacetamide to rat liver protein has been examined. Following administration of 3H- or 14C-labeled thioacetamide, the modified amino acids present in the hepatic cytosolic proteins were isolated by enzymatic digestion and ion-exchange chromatography. Approximately 70% of the radioactivity covalently bound to cytosolic protein was recovered in a compound which upon acid hydrolysis yielded lysine and radiolabeled acetate. Additional studies indicated the structure of this adduct was N-epsilon-acetyllysine.
mesh_terms: D000081:Acetamides / Q000008:administration & dosage*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002852:Chromatography, Ion Exchange; D008401:Gas Chromatography-Mass Spectrometry; D008099:Liver / Q000187:drug effects* / Q000378:metabolism; D008239:Lysine / Q000031:analogs & derivatives / Q000032:analysis; D008297:Male; D011506:Proteins / Q000032:analysis / Q000302:isolation & purification*; D051381:Rats; D013853:Thioacetamide / Q000008:administration & dosage*
chemical_list: D000081:Acetamides; D000596:Amino Acids; D011506:Proteins; D013853:Thioacetamide; C016949:N-epsilon-acetyllysine; D008239:Lysine